Steady state and time-resolved IR spectroscopy of the native and unfolded states of bovine ubiquitin: protein stability and temperature-jump kinetic measurements of protein folding at low pH

  • Colley C
  • Griffiths-Jones S
  • George M
 et al. 
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Abstract

Infrared spectroscopy has been used to characterise the folded and unfolded states of bovine ubiquitin (a small protein of 76 residues) under acidic conditions (pH 1); fast time-resolved measurements of protein unfolding, initiated by a laser-induced temperature-jump of 8 °C, shows rapid refolding and β-sheet secondary structure formation on a timescale of a few milliseconds.

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Authors

  • Christopher S. Colley

  • Samuel R. Griffiths-Jones

  • Michael W. George

  • Mark S. Searle

  • Ian P. Clark

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